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        <identifier>oai:www.ideals.illinois.edu:2142/19323</identifier>
        <datestamp>2023-07-10</datestamp>
        <setSpec>col_2142_5131</setSpec>
        <setSpec>col_2142_14828</setSpec>
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        <thesis xmlns="http://www.ndltd.org/standards/metadata/etdms/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:dc="http://purl.org/dc/elements/1.1/" xsi:schemaLocation="http://www.ndltd.org/standards/metadata/etdms/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdms11.xsd http://purl.org/dc/elements/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdmsdc.xsd">
          <dc:contributor>Crofts, Antony R.</dc:contributor>
          <dc:creator>Wang, Zhenggan</dc:creator>
          <dc:date>2011-05-07T12:03:54Z</dc:date>
          <dc:date>2011-05-07T12:03:54Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>1990</dc:date>
          <dc:description>The kinetics and thermodynamics of the high potential chain in the chromatophores from Rhodobacter sphaeroides have been reexamined. It was found that RC, cyt c$\sb2$ and c$\sb1$ after a flash reached a state not far from the expected ideal equilibrium under the conditions of our experiments.</dc:description>
          <dc:description>An extinction coefficient for cyt b$\sb{\rm H}$ was computed from comparison of oxidation kinetics of c cytochromes in the presence of antimycin and UHDBT. The effects of myxothiazol on the cyt c oxidation have also been discussed.</dc:description>
          <dc:description>Our observations of the temperature dependence of cyt b reduction suggested that quinone diffusion was more rapid than turnover of the bc$\sb1$ complex, and that the chemical step of quinol oxidation was the rate-limiting step in the photosynthetic electron transport of chromatophore system.</dc:description>
          <dc:description>Oxidation kinetic of quinol by bc$\sb1$ complex in chromatophores was simulated. A set of kinetic parameters were obtained from optimization, and compared with experimental results. A minimal model of quinol oxidation was proposed, and discussed under the context of the Q-cycle mechanism.</dc:description>
          <dc:description>Made available in DSpace on 2011-05-07T12:03:54Z (GMT). No. of bitstreams: 2
license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5)
9026347.pdf: 5107740 bytes, checksum: 9b8555e980c9de07dfcf0a88a5fd8290 (MD5)
  Previous issue date: 1990</dc:description>
          <dc:description>Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:36:10Z
Item is restricted indefinitely.</dc:description>
          <dc:description>Restriction data tranferred 2014-07-01T11:14:31-05:00
Original Data
Group with Access UIUC Users [automated]
Release Date: none
Reason: ETDs are only available to UIUC Users without author permission</dc:description>
          <dc:description>ETDs are only available to UIUC Users without author permission</dc:description>
          <dc:description>U of I Only</dc:description>
          <dc:identifier>AAI9026347</dc:identifier>
          <dc:identifier>(UMI)AAI9026347</dc:identifier>
          <dc:identifier>http://hdl.handle.net/2142/19323</dc:identifier>
          <dc:language>eng</dc:language>
          <dc:rights>Copyright 1990 Wang, Zhenggan</dc:rights>
          <dc:subject>Biophysics, General</dc:subject>
          <dc:title>Quinol oxidation by the ubiquinol:cytochrome c(2) oxidoreductase in the chromatophores from Rhodobacter sphaeroides</dc:title>
          <dc:type>text</dc:type>
          <degree>
            <department>Biophysics and Computational Biology</department>
            <discipline>Biophysics</discipline>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
          </degree>
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